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10.1002/iub.2359 http://scihub22266oqcxt.onion/10.1002/iub.2359 32812340!7461454!32812340     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       IUBMB+Life 2020 ; 72 (10): 2112-2120 Nephropedia Template TP {{tp|p=32812340|t=2020. Vitamin B12 may inhibit RNA-dependent-RNA polymerase activity of nsp12 from the SARS-CoV-2 virus |pdf=|usr=}}{{32812340}} gab.com Text Vitamin B12 may inhibit RNA-dependent-RNA polymerase activity of nsp12 from the SARS-CoV-2 virus JO: IUBMB Life http://www.kidney.de/pget.php?&tw=1&pmid=32812340 #FOAvip SARS-CoV-2 is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. Like other members of this family, the virus possesses a positive-sense single-stranded RNA genome. The genome encodes for the nsp12 protein, which houses the RNA-dependent-RNA polymerase (RdRP) activity responsible for the replication of the viral genome. A homology model of nsp12 was prepared using the structure of the SARS nsp12 (6NUR) as a model. The model was used to carry out in silico screening to identify molecules among natural products, or Food and Drug Administration-approved drugs that can potentially inhibit the activity of nsp12. This exercise showed that vitamin B12 (methylcobalamin) may bind to the active site of the nsp12 protein. A model of the nsp12 in complex with substrate RNA and incoming NTP showed that vitamin B12 binding site overlaps with that of the incoming nucleotide. A comparison of the calculated energies of binding for RNA plus NTP and methylcobalamin suggested that the vitamin may bind to the active site of nsp12 with significant affinity. It is, therefore, possible that methylcobalamin binding may prevent association with RNA and NTP and thus inhibit the RdRP activity of nsp12. Overall, our computational studies suggest that methylcobalamin form of vitamin B12 may serve as an effective inhibitor of the nsp12 protein. Twit Text FOAVip Vitamin B12 may inhibit RNA-dependent-RNA polymerase activity of nsp12 from the SARS-CoV-2 virus ????IUBMB Life http://www.kidney.de/pget.php?&tw=1&pmid=32812340 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32812340 #FOAvip English Wikipedia <ref>{{Cite pmid|32812340}}</ref> Vitamin B12 may inhibit RNA-dependent-RNA polymerase activity of nsp12 from the SARS-CoV-2 virus #MMPMID32812340 Narayanan N; Nair DT IUBMB Life 2020[Oct]; 72 (10): 2112-2120 PMID32812340show ga SARS-CoV-2 is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. Like other members of this family, the virus possesses a positive-sense single-stranded RNA genome. The genome encodes for the nsp12 protein, which houses the RNA-dependent-RNA polymerase (RdRP) activity responsible for the replication of the viral genome. A homology model of nsp12 was prepared using the structure of the SARS nsp12 (6NUR) as a model. The model was used to carry out in silico screening to identify molecules among natural products, or Food and Drug Administration-approved drugs that can potentially inhibit the activity of nsp12. This exercise showed that vitamin B12 (methylcobalamin) may bind to the active site of the nsp12 protein. A model of the nsp12 in complex with substrate RNA and incoming NTP showed that vitamin B12 binding site overlaps with that of the incoming nucleotide. A comparison of the calculated energies of binding for RNA plus NTP and methylcobalamin suggested that the vitamin may bind to the active site of nsp12 with significant affinity. It is, therefore, possible that methylcobalamin binding may prevent association with RNA and NTP and thus inhibit the RdRP activity of nsp12. Overall, our computational studies suggest that methylcobalamin form of vitamin B12 may serve as an effective inhibitor of the nsp12 protein. |*Genome, Viral[MESH] |Amino Acid Sequence[MESH] |Antiviral Agents/chemistry/*pharmacology[MESH] |Binding Sites[MESH] |Coronavirus RNA-Dependent RNA Polymerase/*antagonists & inhibitors/chemistry/genetics/metabolism[MESH] |High-Throughput Screening Assays[MESH] |Molecular Docking Simulation[MESH] |Molecular Dynamics Simulation[MESH] |Prescription Drugs/chemistry/pharmacology[MESH] |Protein Binding[MESH] |Protein Conformation, alpha-Helical[MESH] |Protein Conformation, beta-Strand[MESH] |Protein Interaction Domains and Motifs[MESH] |SARS-CoV-2/drug effects/*enzymology/genetics[MESH] |Sequence Alignment[MESH] |Sequence Homology, Amino Acid[MESH] |Substrate Specificity[MESH] |Thermodynamics[MESH] |User-Computer Interface[MESH]Vitamin B12 may inhibit RNA-dependent-RNA polymerase activity of nsp12(epmc).pdf DeepDyve Pubget Overpricing